Clathrin adaptors drive phase separation in endocytosis and trafficking.

Clathrin adaptors Ent5 and Sla2 drive phase separation essential for membrane trafficking, with Ent5's helix and Sla2's coiled-coil mediating condensate formation.

• Why it matters: Understanding how adaptor proteins contribute to biomolecular condensates clarifies mechanisms underlying endocytosis and trafficking, which are vital for cellular function and health.
• What they did: The study examined two yeast adaptors, Ent5 and Sla2, demonstrating their ability to undergo liquid-liquid phase separation in vitro and in vivo, with specific structural regions responsible for this behavior.
• The result: Disruption of Ent5's helix delays transport events, highlighting phase separation's role in trafficking efficiency, and revealing distinct structural features that couple clathrin binding with membrane association.